High-intensity interval training remodels the proteome and acetylome of human skeletal muscle.

High-intensity interval training remodels the proteome and acetylome of human skeletal muscle.
复制标题

高强度间隔训练重塑了人骨骼肌的蛋白质组和乙酰基组。

DOI:
10.7554/elife.69802
复制
发表时间:
2022-05-31
期刊:
影响因子:
7.7
通讯作者:
James, David E.
James, David E.
中科院分区:
生物学1区
文献类型:
--
作者:
Hostrup, Morten;Lemminger, Anders Krogh;Stocks, Ben;Gonzalez-Franquesa, Alba;Larsen, Jeppe Kjaergaard;Quesada, Julia Prats;Thomassen, Martin;Weinert, Brian Tate;Bangsbo, Jens;Deshmukh, Atul Shahaji;James, David E.

文献摘要

被引文献

相似文献

运动是预防和治疗代谢性疾病的有效策略。骨骼肌蛋白质组的改变,包括翻译后修饰,调节其对运动的代谢适应。在这里,我们研究了高强度间歇训练(HIIT)对人类骨骼肌蛋白质组和乙酰基组的影响,揭示了464个乙酰化蛋白质上的3168个蛋白质和1263个赖氨酸乙酰基位点的反应。我们确定了全球蛋白质适应运动训练参与代谢,兴奋-收缩耦合,和肌原纤维钙敏感性。此外,HIIT增加了线粒体蛋白的乙酰化,特别是那些复杂的V。我们还强调了运动响应组蛋白乙酰化位点的调节。这些数据证明了骨骼肌蛋白质组和乙酰基组的可塑性,为骨骼肌内收缩、代谢和转录过程的调节提供了见解。在这里,我们提供了一个实质性的假设生成资源,以刺激进一步的机制研究,调查运动如何改善代谢健康。
Exercise is an effective strategy in the prevention and treatment of metabolic diseases. Alterations in the skeletal muscle proteome, including post-translational modifications, regulate its metabolic adaptations to exercise. Here, we examined the effect of high-intensity interval training (HIIT) on the proteome and acetylome of human skeletal muscle, revealing the response of 3168 proteins and 1263 lysine acetyl-sites on 464 acetylated proteins. We identified global protein adaptations to exercise training involved in metabolism, excitation-contraction coupling, and myofibrillar calcium sensitivity. Furthermore, HIIT increased the acetylation of mitochondrial proteins, particularly those of complex V. We also highlight the regulation of exercise-responsive histone acetyl-sites. These data demonstrate the plasticity of the skeletal muscle proteome and acetylome, providing insight into the regulation of contractile, metabolic and transcriptional processes within skeletal muscle. Herein, we provide a substantial hypothesis-generating resource to stimulate further mechanistic research investigating how exercise improves metabolic health.